|
Name |
Accession |
Description |
Interval |
E-value |
| DUF3502 |
pfam12010 |
Domain of unknown function (DUF3502); This presumed domain is functionally uncharacterized. ... |
352-483 |
2.75e-50 |
|
Domain of unknown function (DUF3502); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 140 amino acids in length. This domain is found associated with pfam01547.
Pssm-ID: 463429 Cd Length: 131 Bit Score: 167.79 E-value: 2.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 352 GIEGEAWEKVDgsDDKIKLLDGYQPNTHMSAWNTGNNKILYTQESITDDMIAKRDQSIADAETSPILGFSFNTDSVKTEL 431
Cdd:pfam12010 1 GIEGVHYEKVG--DGKIKLLPDGVDAYNPPGWAWGNQFILYLWEGEPPDKWEEFKEFNESAKASPALGFTFDSSPVKNEI 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 488214766 432 SNISNVMNQYLDGLNTGTVDPDETLPKLKDALDKAGYDKVLKEMQKQYDEFR 483
Cdd:pfam12010 79 AACSNVVNEYKPALNTGAVDPEETLPKFNAKLKAAGIDKVIAEKQKQLDAFL 130
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
5-342 |
7.91e-32 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 125.16 E-value: 7.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 5 KKLAFTGVSALLLGtLAACGGSGSkDQAEASNSDTLQMYQIGDKP-DNFDQLMEVANKrieKEIGVKVNINYIGWGDYEK 83
Cdd:COG1653 2 RRLALALAAALALA-LAACGGGGS-GAAAAAGKVTLTVWHTGGGEaAALEALIKEFEA---EHPGIKVEVESVPYDDYRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 84 KMNVIISSGENYDIAF--ANNYVSNAQKGAFADLTELAPKYAEKaYNDLDEAYIKGNLVNGKLYAFPVNGNVfaqQVLTF 161
Cdd:COG1653 77 KLLTALAAGNAPDVVQvdSGWLAEFAAAGALVPLDDLLDDDGLD-KDDFLPGALDAGTYDGKLYGVPFNTDT---LGLYY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 162 NKALLDKYDLSIDgiQSYADAEKVLKEFHEKEPNTaafaigqGFKVQGNFDYPLGNTLP-FAIDLDGDDSKIinQYDNET 240
Cdd:COG1653 153 NKDLFEKAGLDPP--KTWDELLAAAKKLKAKDGVY-------GFALGGKDGAAWLDLLLsAGGDLYDEDGKP--AFDSPE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 241 YIGLLRTMHSWYKQGLIPSDAATSNKDyplEGNTWLMRGET----QGPYDYGdTILTNAAKQEL-VSKAITVPLKSTAQA 315
Cdd:COG1653 222 AVEALEFLKDLVKDGYVPPGALGTDWD---DARAAFASGKAammiNGSWALG-ALKDAAPDFDVgVAPLPGGPGGKKPAS 297
|
330 340
....*....|....*....|....*....
gi 488214766 316 QM--ANFVVSNTSKNKEKSVELLGLLNSD 342
Cdd:COG1653 298 VLggSGLAIPKGSKNPEAAWKFLKFLTSP 326
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
61-481 |
1.41e-31 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270298 [Multi-domain] Cd Length: 471 Bit Score: 126.67 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 61 KRIEKEIGVKVNINYIGWGDYEKKMNVIISSGENYDIAFANNYV---SNAQKGAFADLTELAPKYAEKAYNDLDEAYIKG 137
Cdd:cd13580 26 KYLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNDPQlsiTLVKQGALWDLTDYLDKYYPNLKKIIEQEGWDS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 138 NLVNGKLYAFPVNGNVFAQQVLTFNKALLDKYDLSIDgiQSYADAEKVLKEFHEKEPN----TAAFAIGQGFKVQGNFDY 213
Cdd:cd13580 106 ASVDGKIYGIPRKRPLIGRNGLWIRKDWLDKLGLEVP--KTLDELYEVAKAFTEKDPDgngkKDTYGLTDTKDLIGSGFT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 214 PLGNTL--PFAIDLDGDDSKIINQYDNETYIGLLRTMHSWYKQGLIPSDAATSNKDYPLE----GNTWLMRGETQGPYDY 287
Cdd:cd13580 184 GLFGAFgaPPNNWWKDEDGKLVPGSIQPEMKEALKFLKKLYKEGLIDPEFAVNDGTKANEkfisGKAGIFVGNWWDPAWP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 288 GDTILTNAAKQELVskAITVPL----KSTAQAQMAN---FVVSNTSKNKEKSVELLGLLnSDPELLNGLVWGIEGEAWEK 360
Cdd:cd13580 264 QASLKKNDPDAEWV--AVPIPSgpdgKYGVWAESGVngfFVIPKKSKKPEAILKLLDFL-SDPEVQKLLDYGIEGVHYTV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 361 VDGS----DDKIKLLDGYQPNTHMSAWNTGNNKILYT---------QESITDDMIAKRDQSIADAETS-PILGFSFNTDS 426
Cdd:cd13580 341 KDGGpvniIPPDKQEVGDATLDYFQGSLALEKYKLTNngerksdakKEALDERVVNANDEENENIAVGpPTETLVSPTEK 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 488214766 427 VKTELSNIsnvMNQYLDGLNTGTVdPDETLPKLKDALDKAGYDKVLKEMQKQYDE 481
Cdd:cd13580 421 YGATLDKL---EDDAFTKIIMGQI-PLDEFDKFVEEWKKSGGDEITKEVNEWYKE 471
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
46-342 |
8.82e-11 |
|
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.
Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 62.82 E-value: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 46 GDKPDNFDQLMEVANKRIEKEIGVKVNINYIGWGDYEKKMNVIISSGEN-YDIAFANNYVSN--AQKGAFADLTELAPKY 122
Cdd:pfam01547 1 AASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGpADVFASDNDWIAelAKAGLLLPLDDYVANY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 123 AEKAYndldeayikgnlvnGKLYAFPVNGNvfaQQVLTFNKALLDKYDlsIDGIQSYADAEKVLKEFHEKEPNTAAFAIG 202
Cdd:pfam01547 81 LVLGV--------------PKLYGVPLAAE---TLGLIYNKDLFKKAG--LDPPKTWDELLEAAKKLKEKGKSPGGAGGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 203 QGFKVQGNFDYPLGNTLPfaIDLDGDDSKIINQYDNETYIGLLRTMHSWYKQGLIPSDAATSNKDYPlEGNTWLMRGETQ 282
Cdd:pfam01547 142 DASGTLGYFTLALLASLG--GPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGR-EALALFEQGKAA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488214766 283 GPYDYGDTILTNAAKQELVSKAIT------------VPLKSTAQAQMANFVVSNTSKNKEKSVELLGLLNSD 342
Cdd:pfam01547 219 MGIVGPWAALAANKVKLKVAFAAPapdpkgdvgyapLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSP 290
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
1-166 |
8.53e-03 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 38.45 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 1 MKLWKKLAFTGVSALLLGTLAACggsgskdqaeASNSDTLQMYQIGDKpdNFDQLMEVAnKRIEKEIGVKVNINYIGwgD 80
Cdd:PRK09474 4 KKGLRTLALSALATLMFSASALA----------KIEEGKLVIWINGDK--GYNGLAEVG-KKFEKDTGIKVTVEHPD--K 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 81 YEKKMNVIISSGENYDIAF--ANNYVSNAQKGAFADLT---ELAPKYAEKAYNDLDeayikgnlVNGKLYAFPVNGNVFA 155
Cdd:PRK09474 69 LEEKFPQVAATGDGPDIIFwaHDRFGGYAQSGLLAEVTpskAFKDKLVPFTWDAVR--------YNGKLIGYPIAVEALS 140
|
170
....*....|.
gi 488214766 156 qqvLTFNKALL 166
Cdd:PRK09474 141 ---LIYNKDLV 148
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DUF3502 |
pfam12010 |
Domain of unknown function (DUF3502); This presumed domain is functionally uncharacterized. ... |
352-483 |
2.75e-50 |
|
Domain of unknown function (DUF3502); This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 140 amino acids in length. This domain is found associated with pfam01547.
Pssm-ID: 463429 Cd Length: 131 Bit Score: 167.79 E-value: 2.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 352 GIEGEAWEKVDgsDDKIKLLDGYQPNTHMSAWNTGNNKILYTQESITDDMIAKRDQSIADAETSPILGFSFNTDSVKTEL 431
Cdd:pfam12010 1 GIEGVHYEKVG--DGKIKLLPDGVDAYNPPGWAWGNQFILYLWEGEPPDKWEEFKEFNESAKASPALGFTFDSSPVKNEI 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 488214766 432 SNISNVMNQYLDGLNTGTVDPDETLPKLKDALDKAGYDKVLKEMQKQYDEFR 483
Cdd:pfam12010 79 AACSNVVNEYKPALNTGAVDPEETLPKFNAKLKAAGIDKVIAEKQKQLDAFL 130
|
|
| UgpB |
COG1653 |
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
5-342 |
7.91e-32 |
|
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 125.16 E-value: 7.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 5 KKLAFTGVSALLLGtLAACGGSGSkDQAEASNSDTLQMYQIGDKP-DNFDQLMEVANKrieKEIGVKVNINYIGWGDYEK 83
Cdd:COG1653 2 RRLALALAAALALA-LAACGGGGS-GAAAAAGKVTLTVWHTGGGEaAALEALIKEFEA---EHPGIKVEVESVPYDDYRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 84 KMNVIISSGENYDIAF--ANNYVSNAQKGAFADLTELAPKYAEKaYNDLDEAYIKGNLVNGKLYAFPVNGNVfaqQVLTF 161
Cdd:COG1653 77 KLLTALAAGNAPDVVQvdSGWLAEFAAAGALVPLDDLLDDDGLD-KDDFLPGALDAGTYDGKLYGVPFNTDT---LGLYY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 162 NKALLDKYDLSIDgiQSYADAEKVLKEFHEKEPNTaafaigqGFKVQGNFDYPLGNTLP-FAIDLDGDDSKIinQYDNET 240
Cdd:COG1653 153 NKDLFEKAGLDPP--KTWDELLAAAKKLKAKDGVY-------GFALGGKDGAAWLDLLLsAGGDLYDEDGKP--AFDSPE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 241 YIGLLRTMHSWYKQGLIPSDAATSNKDyplEGNTWLMRGET----QGPYDYGdTILTNAAKQEL-VSKAITVPLKSTAQA 315
Cdd:COG1653 222 AVEALEFLKDLVKDGYVPPGALGTDWD---DARAAFASGKAammiNGSWALG-ALKDAAPDFDVgVAPLPGGPGGKKPAS 297
|
330 340
....*....|....*....|....*....
gi 488214766 316 QM--ANFVVSNTSKNKEKSVELLGLLNSD 342
Cdd:COG1653 298 VLggSGLAIPKGSKNPEAAWKFLKFLTSP 326
|
|
| PBP2_AlgQ_like_1 |
cd13580 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
61-481 |
1.41e-31 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270298 [Multi-domain] Cd Length: 471 Bit Score: 126.67 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 61 KRIEKEIGVKVNINYIGWGDYEKKMNVIISSGENYDIAFANNYV---SNAQKGAFADLTELAPKYAEKAYNDLDEAYIKG 137
Cdd:cd13580 26 KYLEEKTNIDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNDPQlsiTLVKQGALWDLTDYLDKYYPNLKKIIEQEGWDS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 138 NLVNGKLYAFPVNGNVFAQQVLTFNKALLDKYDLSIDgiQSYADAEKVLKEFHEKEPN----TAAFAIGQGFKVQGNFDY 213
Cdd:cd13580 106 ASVDGKIYGIPRKRPLIGRNGLWIRKDWLDKLGLEVP--KTLDELYEVAKAFTEKDPDgngkKDTYGLTDTKDLIGSGFT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 214 PLGNTL--PFAIDLDGDDSKIINQYDNETYIGLLRTMHSWYKQGLIPSDAATSNKDYPLE----GNTWLMRGETQGPYDY 287
Cdd:cd13580 184 GLFGAFgaPPNNWWKDEDGKLVPGSIQPEMKEALKFLKKLYKEGLIDPEFAVNDGTKANEkfisGKAGIFVGNWWDPAWP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 288 GDTILTNAAKQELVskAITVPL----KSTAQAQMAN---FVVSNTSKNKEKSVELLGLLnSDPELLNGLVWGIEGEAWEK 360
Cdd:cd13580 264 QASLKKNDPDAEWV--AVPIPSgpdgKYGVWAESGVngfFVIPKKSKKPEAILKLLDFL-SDPEVQKLLDYGIEGVHYTV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 361 VDGS----DDKIKLLDGYQPNTHMSAWNTGNNKILYT---------QESITDDMIAKRDQSIADAETS-PILGFSFNTDS 426
Cdd:cd13580 341 KDGGpvniIPPDKQEVGDATLDYFQGSLALEKYKLTNngerksdakKEALDERVVNANDEENENIAVGpPTETLVSPTEK 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 488214766 427 VKTELSNIsnvMNQYLDGLNTGTVdPDETLPKLKDALDKAGYDKVLKEMQKQYDE 481
Cdd:cd13580 421 YGATLDKL---EDDAFTKIIMGQI-PLDEFDKFVEEWKKSGGDEITKEVNEWYKE 471
|
|
| PBP2_AlgQ_like_2 |
cd13581 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
61-481 |
1.37e-21 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270299 [Multi-domain] Cd Length: 490 Bit Score: 97.39 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 61 KRIEKEIGVKVNINYIGWGDYEKKMNVIISSGENYDiAFANNYVSNA------QKGAFADLTELAPKYAEKAYNDLDE-A 133
Cdd:cd13581 24 KRLEEKTGIKIEWETVPEDAWAEKKNLMLASGDLPD-AFLGAGASDAdlmtygKQGLFLPLEDLIDKYAPNLKALFDEnP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 134 YIKGNLVN--GKLYAFP-VNGNVFAQ--QVLTFNKALLDKYDLSIDgiQSYADAEKVLKEFHEKEPNTAAFAIGQGF--- 205
Cdd:cd13581 103 DIKAAITApdGHIYALPsVNECYHCSygQRMWINKKWLDKLGLEMP--TTTDELYEVLKAFKEQDPNGNGKADEIPLsfs 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 206 KVQGNFDYPLGNTLPFAID--------LDGDDSKIINQYDNETYIGLLRTMHSWYKQGLIPSDAATSNkdypleGNTWLM 277
Cdd:cd13581 181 GLNGGTDDPAFLLNSFGINdggyggygFVVKDGKVIYTATDPEYKEALAYLNKLYKEGLIDPEAFTQD------YDQLAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 278 RGETQGP-------YDYGDTILTNAAKQELVSKAITVPLKSTAQAQM-------ANFVVSNTSKNKEKSVELLGLLnSDP 343
Cdd:cd13581 255 KGKASTAkvgvffgWDPGLFFGEERYEQYVPLPPLKGPNGDQLAWVGnssgygrGGFVITSKNKNPEAAIRWADFL-YSP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 344 ELLNGLVWGIEGEAWEKVDGSDDKIKLLDGYQPNTHMSAWNTGNNKILYTQESITDD-------------MIAKRDQS-- 408
Cdd:cd13581 334 EGSLQANFGPEGEDWEKNPDGEYGVDGPPAAYKILEPSEGEQNVAWADGGPGAIPDEyrlkqvtdedmdeAEARLDEAkk 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488214766 409 -IADAETSPILGFSFNTDSVKTELS----NISNVMNQYLDGLNTGTVDpDETLPKLKDALDKAGYDKVLKEMQKQYDE 481
Cdd:cd13581 414 yYEPYAPPDNSPPPALLDEEAEKIStiqtDINNYIEQKRAKFITGGGD-DKEWDAYVKQLEKMGLDEYLEIYQKAYDR 490
|
|
| PBP2_TMBP_like |
cd13585 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
64-342 |
4.97e-20 |
|
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270303 [Multi-domain] Cd Length: 383 Bit Score: 91.70 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 64 EKEIGVKVNINYIGWGDYEKKMNVIISSGENYDIAFANN-YVSN-AQKGAFADLTELAPKYAEKAynDLDEAYIKGNLVN 141
Cdd:cd13585 25 KENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGpWVPEfASNGALLDLDDYIEKDGLDD--DFPPGLLDAGTYD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 142 GKLYAFPVNGNVfaqQVLTFNKALLDKYDLSIDGIQSYADAEKVLKEFHEKEPNTAAFAIGQGFKVQGNFD-YPLGNTLP 220
Cdd:cd13585 103 GKLYGLPFDADT---LVLFYNKDLFDKAGPGPKPPWTWDELLEAAKKLTDKKGGQYGFALRGGSGGQTQWYpFLWSNGGD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 221 FaidLDGDDSKIinQYDNETYIGLLRTMHSWYKQGLIPSDAATSNKDypleGNTWLMRGET----QGPYDYGdtiltNAA 296
Cdd:cd13585 180 L---LDEDDGKA--TLNSPEAVEALQFYVDLYKDGVAPSSATTGGDE----AVDLFASGKVammiDGPWALG-----TLK 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488214766 297 KQELVSKAITVPL------KSTAQAQMANFVVSNTSKNKEKSVELLGLLNSD 342
Cdd:cd13585 246 DSKVKFKWGVAPLpagpggKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSK 297
|
|
| PBP2_AlgQ_like |
cd13521 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
61-481 |
1.96e-19 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270239 [Multi-domain] Cd Length: 483 Bit Score: 90.98 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 61 KRIEKEIGVKVNINYIGWGDYEKKMNVIISSGENYDIAFA----NNYVSNAQKGAFADLTELAPKYAE-KAYNDLDEAYI 135
Cdd:cd13521 24 KEIEKLTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGAdylkDKFIAYGMEGAFLPLSKYIDQYPNlKAFFKQHPDVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 136 KGNL-VNGKLYAFP-VNGNVFAQQVLTFNKALLDKYDLSIdgIQSYADAEKVLKEFHEKEPN-----------TAAFAIG 202
Cdd:cd13521 104 RASTaSDGKIYLIPyEPPKDVPNQGYFIRKDWLDKLNLKT--PKTLDELYNVLKAFKEKDPNgngkadeipfiDRDPLYG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 203 QGFKVQGNFDYPLGNTLPFaiDLDGDDSKIINQYDNETYIGLLRTMHSWYKQGLIPSDAATSNKDYPLE----GNTWLMr 278
Cdd:cd13521 182 AFRLINSWGARSAGGSTDS--DWYEDNGKFKHPFASEEYKDGMKYMNKLYTEGLIDKESFTQKDDQAEQkfsnGKLGGF- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 279 geTQGPYDYGDTILTNAAKQELVSKAITVPLKSTAQAQMAN----------FVVSNTSKNKEKSVELLGLLNSDP--ELL 346
Cdd:cd13521 259 --THNWFASDNLFTAQLGKEKPMYILLPIAPAGNVKGRREEdspgytgpdgVAISKKAKNPVAALKFFDWLASEEgrELA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 347 NglvWGIEGEAWEKVDG-----SDDKIKLLDGYQPNTHMSA------WNTGNNKILYTQESITD------DMIAKRDQSI 409
Cdd:cd13521 337 N---FGIEGVHYNKDNGkkrtkDPVKKSDQPGDNQLYDLPAfikggfWNEYTYPRPQWGVLTGDsarlpiDMYIKPKYSP 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488214766 410 ADAETSPILgfSFNTDSVKTELSNISNVMNQYLDGLNTGTVDPDETLPKLKDALDKAGYDKVLKEMQKQYDE 481
Cdd:cd13521 414 PKPEGANLT--IEEREQVSIDNTELKDIMMEMTQKWIMGTKEKDEEWDAYQEQLKSAGLYQVTEEVQKAYDR 483
|
|
| MalE |
COG2182 |
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-342 |
2.56e-18 |
|
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 86.93 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 1 MKLwKKLAFTGVSALLLGTLAACGGSGSKDQ--AEASNSDTLQMYQIGDKPDNFDQlmevANKRIEKEIGVKVNINYIGW 78
Cdd:COG2182 1 MKR-RLLAALALALALALALAACGSGSSSSGssSAAGAGGTLTVWVDDDEAEALEE----AAAAFEEEPGIKVKVVEVPW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 79 GDYEKKMNVIISSGENYDIA-FANNYVSN-AQKGAFADLTELApkyaeKAYNDLDEAYIKGNLVNGKLYAFPVNGNVFAq 156
Cdd:COG2182 76 DDLREKLTTAAPAGKGPDVFvGAHDWLGElAEAGLLAPLDDDL-----ADKDDFLPAALDAVTYDGKLYGVPYAVETLA- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 157 qvLTFNKALLDKYDlsidgIQSYADAEKVLKEFHEKEPNTAAFAIGQGFkvqgnFDYPL----GNTLpfaIDLDGDDSKI 232
Cdd:COG2182 150 --LYYNKDLVKAEP-----PKTWDELIAAAKKLTAAGKYGLAYDAGDAY-----YFYPFlaafGGYL---FGKDGDDPKD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 233 INqYDNETYIGLLRTMHSWYKQGLIPSDAATSN-KDYPLEGNTWLMRGetqGPYDYGDtiltnaAKQELVSKAITVPL-K 310
Cdd:COG2182 215 VG-LNSPGAVAALEYLKDLIKDGVLPADADYDAaDALFAEGKAAMIIN---GPWAAAD------LKKALGIDYGVAPLpT 284
|
330 340 350
....*....|....*....|....*....|....*...
gi 488214766 311 STAQAQMANFV------VSNTSKNKEKSVELLGLLNSD 342
Cdd:COG2182 285 LAGGKPAKPFVgvkgfgVSAYSKNKEAAQEFAEYLTSP 322
|
|
| PBP2_AlgQ1_2 |
cd13584 |
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ... |
61-480 |
1.18e-14 |
|
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 periplasmic binding fold; This group represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria such as Sphingomonas sp. A1. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that includes alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270302 [Multi-domain] Cd Length: 481 Bit Score: 75.94 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 61 KRIEKEIGVKVNI--NYIGWGDYEKkMNVIISSGENYDIAFANN--YVSNAQK----GAFADLTELAPKYAE--KAYNDL 130
Cdd:cd13584 24 KEMERKTNVKLNFvaNPVAQNSQEQ-FNLMMASGQLPDIIGGDWlkDKGGFEKygedGAFLPLNDLIDQYAPnlKKFLDE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 131 DEAYIKGNLV-NGKLYAFP-VNGNVFAQQ--VLTFNKALLDKYDLSIDgiQSYADAEKVLKEFHEKEPNtaafaiGQGFK 206
Cdd:cd13584 103 HPDVKKAITTdDGNIYGFPyLPDGDVAKEarGYFIRKDWLDKLGLKTP--STIDEWYTVLKAFKERDPN------GNGKA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 207 VQgnfdYPLGNTLPfAIDLDG--------------DDSKIINQYDNETYIGLLRTMHSWYKQGLIPSDAATsNKDYPLEG 272
Cdd:cd13584 175 DE----VPLILTKP-GYDETGrlinawgaymdfyqENGKVKYGPLEPGFKDFLKTMNQWYKEGLIDPDFFT-RKAKAREQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 273 NtwLMRGETQG--------PYDYGDTILTNAAKQELVskAITVPLKSTAQAQM----------ANFVVSNTSKNKEKSVE 334
Cdd:cd13584 249 N--IMNGNIGGfthdwfasTGTFNLALLKNVPDFKLV--AVPPPVLNKGQTPYeedsrqiakgDGAAITASNKNPVLAIK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 335 LLGLLNSDP--ELLNglvWGIEGEAWEKVDG----SDDKIKllDGYQPNTHMSAWNTGNNKILYTQESITDDMIAKRDQ- 407
Cdd:cd13584 325 WLDYAYSEEgrLLSN---FGVEGESYTIKNGkpvfTDDVLK--DPQPLVNALSLYYGAQIPGGFWQDYEYEEQWTTPEAl 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 408 ---SIADAETSPILGFSF-NTDSVKTELSNISNVMNQYLD----GLNTGTVDPDETLPKLKDALDKAGYDKVLKEMQKQY 479
Cdd:cd13584 400 eskDIYAKNKYVMPLPPVtLTEEERSIYDSIMTDIDTYVNemgqKWIMGKEDADDNWDEYQKKLKSLGLYEALEIQQAAY 479
|
.
gi 488214766 480 D 480
Cdd:cd13584 480 D 480
|
|
| PBP2_AlgQ_like_4 |
cd13583 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
61-382 |
2.03e-12 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270301 [Multi-domain] Cd Length: 478 Bit Score: 68.92 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 61 KRIEKEIGVKVNINYIGWGDYEKKMNVIISSGENYDIAFANNYVSNAQKGA------FADLTELAPKYaEKAYNDLDEAY 134
Cdd:cd13583 24 KEIEEKTNVKFKRTPIPSSDYETKRSLLIASGDAPDIIPVLYPGEENEFVAsgallpISDYLDYMPNY-KKYVEKWGLGK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 135 IK--GNLVNGKLYAFPV-NGNVFAQQVLTFNKALLDKYDLSIDgiQSYADAEKVLKEFHEKEPNTAAFAIGQGFKVQGN- 210
Cdd:cd13583 103 ELatGRQSDGKYYSLPGlHEDPGVQYSFLYRKDIFEKAGIKIP--TTWDEFYAALKKLKEKYPDSYPYSDRWNSNALLLi 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 211 ----FDYPLGNTLPFAIdLDGDDSKIINQYDNETYIGLLRTMHSWYKQGLIPSDAATSNKD----YPLEGNTWLMRGETQ 282
Cdd:cd13583 181 aapaFGTTAGWGFSNYT-YDPDTDKFVYGATTDEYKDMLQYFNKLYAEGLLDPESFTQTDDqakaKFLNGKSFVITTNPQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 283 GPYDYgDTILTNAAKQELVSKAITVPLKSTAQAQMAN-----FVVS---NTSKNKEKSVELLGLLNSdPELLNGLVWGIE 354
Cdd:cd13583 260 TVDEL-QRNLRAADGGNYEVVSITPPAGPAGKAINGSrlengFMISskaKDSKNFEALLQFLDWLYS-DEGQELATWGVE 337
|
330 340
....*....|....*....|....*...
gi 488214766 355 GEAWEKVDgsDDKIKLLDGYQPNTHMSA 382
Cdd:cd13583 338 GETYTKEG--DGKVYLADSNTPALNPSG 363
|
|
| SBP_bac_1 |
pfam01547 |
Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
46-342 |
8.82e-11 |
|
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.
Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 62.82 E-value: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 46 GDKPDNFDQLMEVANKRIEKEIGVKVNINYIGWGDYEKKMNVIISSGEN-YDIAFANNYVSN--AQKGAFADLTELAPKY 122
Cdd:pfam01547 1 AASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGpADVFASDNDWIAelAKAGLLLPLDDYVANY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 123 AEKAYndldeayikgnlvnGKLYAFPVNGNvfaQQVLTFNKALLDKYDlsIDGIQSYADAEKVLKEFHEKEPNTAAFAIG 202
Cdd:pfam01547 81 LVLGV--------------PKLYGVPLAAE---TLGLIYNKDLFKKAG--LDPPKTWDELLEAAKKLKEKGKSPGGAGGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 203 QGFKVQGNFDYPLGNTLPfaIDLDGDDSKIINQYDNETYIGLLRTMHSWYKQGLIPSDAATSNKDYPlEGNTWLMRGETQ 282
Cdd:pfam01547 142 DASGTLGYFTLALLASLG--GPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVAGADGR-EALALFEQGKAA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488214766 283 GPYDYGDTILTNAAKQELVSKAIT------------VPLKSTAQAQMANFVVSNTSKNKEKSVELLGLLNSD 342
Cdd:pfam01547 219 MGIVGPWAALAANKVKLKVAFAAPapdpkgdvgyapLPAGKGGKGGGYGLAIPKGSKNKEAAKKFLDFLTSP 290
|
|
| SBP_bac_8 |
pfam13416 |
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
61-331 |
1.23e-09 |
|
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.
Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 58.96 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 61 KRIEKEIGVKVNINYIGWGDYEKKMNVIISSGENYDIAFANNYvsNAQKGAFADLTELAPKYAEKAYNDLDEaYIKGNLV 140
Cdd:pfam13416 4 KAFEKKTGVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVVWIA--ADQLATLAEAGLLADLSDVDNLDDLPD-ALDAAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 141 NGKLYAFPVNGNvfAQQVLTFNKALLDKydlSIDGIQSYADAEKVLKEFHEKepntaafaigqgfkvQGNFDYPLGNTLP 220
Cdd:pfam13416 81 DGKLYGVPYAAS--TPTVLYYNKDLLKK---AGEDPKTWDELLAAAAKLKGK---------------TGLTDPATGWLLW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 221 FAIDLDGDDSKIINqyDNETYIGLLRTMHSWYKQGLIPSDAATSNKDYpLEGNTWLMRGetqGPYDYGDTIltnAAKQEL 300
Cdd:pfam13416 141 ALLADGVDLTDDGK--GVEALDEALAYLKKLKDNGKVYNTGADAVQLF-ANGEVAMTVN---GTWAAAAAK---KAGKKL 211
|
250 260 270
....*....|....*....|....*....|.
gi 488214766 301 VskaiTVPLKSTAQAQMANFVVSNTSKNKEK 331
Cdd:pfam13416 212 G----AVVPKDGSFLGGKGLVVPAGAKDPRL 238
|
|
| PBP2_AlgQ_like_3 |
cd13582 |
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
39-481 |
2.15e-08 |
|
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.
Pssm-ID: 270300 [Multi-domain] Cd Length: 504 Bit Score: 56.56 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 39 TLQMY--QIGDKPDNFDQlmEVAnKRIEKEIGVKVNINYIGwGDYEKKMNVIISSGENYDIAFANNyvsNAQK----GAF 112
Cdd:cd13582 3 TFTFFsaDSNATPDDFKT--PVA-KKITELTGVTLEIEYLV-GGEKQKIGLMIASGDLPDLIYAKG---DTDKlieaGAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 113 ADLTELAPKYA---EKAYNDLDEAYIKGNlvNGKLYAFP---VNGNVFAQQ-VLTFNKALLDkyDLSIDGIQSYADAEKV 185
Cdd:cd13582 76 VPLDDLIEKYGpniKKWYGDYLLKKLRSE--DGHIYYLPnyrVEDAPWYPNgGFWLQHDVLK--ELGYPKIKTLDDYENL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 186 LKEFHEKEPN-----TAAF-AIGQGFKVQGNFDYPLGNTLPFAID---LDGDDSKIINQYDNETYIGLLRTMHSWYKQGL 256
Cdd:cd13582 152 IKDYKKKYPTingqpTIGFtALTDDWRFLISVTNPAFLAGYPNDGevyVDPKTLKAKFHYTRPYYKEYYKWLNELWNEGL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 257 IPSDAATSNKDyplegnTWLMR---GETQGPYDYG-------DTILTNAAKQELVSKAITVPLKSTAQA------QMANF 320
Cdd:cd13582 232 LDKESFTQKYD------QYLAKiasGRVLGFYDAGwdignaiTALKAKGKDERLYAYYPVAVGVDDKDYnygdpgYLGGD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 321 VVSNTSKNK--EKSVELLGLLNSdPELLNGLVWGIEGEAWEKVDG-----SDDKIKLLDG--YQPNTHMSAWN------- 384
Cdd:cd13582 306 GIAITKSCKdpERAFKFLDWLAS-EEAQKLINWGIEGVDYDVDDGkrvylTEEMAAKNKDpdYTKKTGIGKYWyfpprkg 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 385 ------TGNNKILYTQESITDDMIAKRDQSIADAETSPILGFSFNTDSVKT--ELSNISN------VMNQYLDGLNTGTV 450
Cdd:cd13582 385 gkfsdgTGNSPTPDPEEEYIYTAVEKKVKAAYKAELWKDMFPPFEEFPVKPygYAWPIGIpdesiaIINQKASDITRKYI 464
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 488214766 451 ---------DPDETLPKLKDALDKAGYDKVLKEMQKQYDE 481
Cdd:cd13582 465 pkaimakpdDFDSIWDEYLKDLEKAGYKKLEEYYTKQIKE 504
|
|
| PBP2_UgpB |
cd14748 |
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
68-174 |
2.70e-08 |
|
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270451 [Multi-domain] Cd Length: 385 Bit Score: 55.76 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 68 GVKVNINYIGWGDYEK-KMNVIISSGENYDIA--FANNYVSNAQKGAFADLTELAPKYAEKAyNDLDEAYIKGNLVNGKL 144
Cdd:cd14748 29 DIKVKAVYQGSYDDTLtKLLAALAAGTAPDVAqvDASWVAQLADSGALEPLDDYIDKDGVDD-DDFYPAALDAGTYDGKL 107
|
90 100 110
....*....|....*....|....*....|
gi 488214766 145 YAFPVNGNVfaqQVLTFNKALLDKYDLSID 174
Cdd:cd14748 108 YGLPFDTST---PVLYYNKDLFEEAGLDPE 134
|
|
| PBP2_TMBP |
cd14750 |
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
112-344 |
5.18e-08 |
|
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270453 [Multi-domain] Cd Length: 385 Bit Score: 54.99 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 112 FAD---LTELAPKYAEKAYNDLDEAYIKGNLVNGKLYAFPVNGNVfaqQVLTFNKALLDKYDLSI----DGIqsYADAEK 184
Cdd:cd14750 72 FAEagwLLPLTEYLKEEEDDDFLPATVEANTYDGKLYALPWFTDA---GLLYYRKDLLEKYGPEPpktwDEL--LEAAKK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 185 VLKefheKEPNTAAFaIGQGFKVQG---NFD---YPLGNTLpfaidLDGDDSKIInqYDNETYIGLLRTMHSWYKQGLIP 258
Cdd:cd14750 147 RKA----GEPGIWGY-VFQGKQYEGlvcNFLellWSNGGDI-----FDDDSGKVT--VDSPEALEALQFLRDLIGEGISP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 259 SDAAT-----SNKDYPlEGNTWLMRGetqGPYDYGdtiLTNAAKQELVSKAITVPLKSTAQAQMA------NFVVSNTSK 327
Cdd:cd14750 215 KGVLTygeeeARAAFQ-AGKAAFMRN---WPYAYA---LLQGPESAVAGKVGVAPLPAGPGGGSAstlggwNLAISANSK 287
|
250
....*....|....*..
gi 488214766 328 NKEKSVELLGLLNSDPE 344
Cdd:cd14750 288 HKEAAWEFVKFLTSPEV 304
|
|
| PBP2_MalE |
cd14747 |
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
39-342 |
1.20e-07 |
|
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270450 [Multi-domain] Cd Length: 386 Bit Score: 53.86 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 39 TLQMYQIGDKPDnfDQLMEVANKRIEKE-IGVKVNINYIGWGDYEKKMNVIISSGENYDIA-FANNYVSN-AQKGAFADL 115
Cdd:cd14747 1 TLTVWAMGNSAE--AELLKELADEFEKEnPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVqLGNTWVAEfAAMGALEDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 116 TelaPKYAEKaynDLDEAYIKGN----LVNGKLYAFPVngnVFAQQVLTFNKALLDKYDLSIDgIQSYADAEKVLKEFHE 191
Cdd:cd14747 79 T---PYLEDL---GGDKDLFPGLvdtgTVDGKYYGVPW---YADTRALFYRTDLLKKAGGDEA-PKTWDELEAAAKKIKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 192 KEPNTAAFAIGQGFKVQGNFdyplgntLPFAIDLDGDdskIINQYDN-------ETYIGlLRTMHSWYKQGLIPSDAATS 264
Cdd:cd14747 149 DGPDVSGFAIPGKNDVWHNA-------LPFVWGAGGD---LATKDKWkatldspEAVAG-LEFYTSLYQKGLSPKSTLEN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 265 nkdyplEGNTW--LMRGET----QGPYDYGDtilTNAAKQELVSKAITVPLKSTAQAQMANF------VVSNTSKNKEKS 332
Cdd:cd14747 218 ------SADVEqaFANGKVamiiSGPWEIGA---IREAGPDLAGKWGVAPLPGGPGGGSPSFaggsnlAVFKGSKNKDLA 288
|
330
....*....|
gi 488214766 333 VELLGLLNSD 342
Cdd:cd14747 289 WKFIEFLSSP 298
|
|
| PBP2_GacH |
cd14751 |
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
55-343 |
5.47e-06 |
|
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270454 [Multi-domain] Cd Length: 376 Bit Score: 48.53 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 55 LMEVANKRIEKEI-GVKVNINYIGWGDYEKKMNVIISSGENYDIAFAN-NYVSNAQK-GAFADLTELAPKYAEKAYndLD 131
Cdd:cd14751 15 LYEKLIPAFEKEYpKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADiAWVPEFAKlGYLQPLDGTPAFDDIVDY--LP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 132 EAyIKGNLVNGKLYAFPVNGNVFAqqvLTFNKALLDkydlsidgiQSYADAEKVLKEFHekepnTAAFAIGQGFKVQGNF 211
Cdd:cd14751 93 GP-METNRYNGHYYGVPQVTNTLA---LFYNKRLLE---------EAGTEVPKTMDELV-----AAAKAIKKKKGRYGLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 212 DYPLG--NTLPFAIDLDG---DDSKIINQYDNETYIGLLRTMHSWYKQGLIPSDAATSnkdyplEGNTW--LMRGE---- 280
Cdd:cd14751 155 ISGDGpyWLLPFLWSFGGdltDEKKATGYLNSPESVRALETIVDLYDEGAITPCASGG------YPNMQdgFKSGRyami 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488214766 281 TQGPYDYGDtILTNAAKQELVSKAIT-VPLKSTAQAQMA---NFVVSNTSKNKEKSVELLGLLNSDP 343
Cdd:cd14751 229 VNGPWAYAD-ILGGKEFKDPDNLGIApVPAGPGGSGSPVggeDLVIFKGSKNKDAAWKFVKFMSSAE 294
|
|
| PBP2_CMBP |
cd13658 |
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
40-258 |
3.68e-04 |
|
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270376 [Multi-domain] Cd Length: 372 Bit Score: 42.86 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 40 LQMYQIGDKPDNFdqlMEVANKRIEKEIGVKVNINYIGWGDYEKKMNVIISSGENYDIAFA--NNYVSNAQKGAFADLte 117
Cdd:cd13658 2 LTVWVDEDKKMAF---IKKIAKQYTKKTGVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAphDRIGSAVLQGLLSPI-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 118 lapKYAEKAYNDLDEAYIKGNLVNGKLYAFPVngnVFAQQVLTFNKALLDkydlsiDGIQSYADAEKVLKEFHEKEPNTA 197
Cdd:cd13658 77 ---KLSKDKKKGFTDQALKALTYDGKLYGLPA---AVETLALYYNKDLVK------NAPKTFDELEALAKDLTKEKGKQY 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488214766 198 AFAigqgFKVqGNFDYplgnTLPFaidLDGDDSKIINQYDNETY---IGL--------LRTMHSWYKQGLIP 258
Cdd:cd13658 145 GFL----ADA-TNFYY----SYGL---LAGNGGYIFKKNGSDLDindIGLnspgavkaVKFLKKWYTEGYLP 204
|
|
| PBP2_Maltodextrin |
cd13657 |
The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
52-182 |
5.39e-04 |
|
The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270375 [Multi-domain] Cd Length: 368 Bit Score: 42.36 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 52 FDQLMEVANKRIEKEigvKVNINYIGWGDYEKKMNVIISSGENYDI-AFANNYVSN-AQKGAFADLTELApkyAEKAYND 129
Cdd:cd13657 16 LQQIIDEFEAKYPVP---NVKVPFEKKPDLQNKLLTAIPAGEGPDLfIWAHDWIGQfAEAGLLVPISDYL---SEDDFEN 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488214766 130 LDEAYIKGNLVNGKLYAFPVNGNVFAqqvLTFNKALLDKYDLSIDGIQSYADA 182
Cdd:cd13657 90 YLPTAVEAVTYKGKVYGLPEAYETVA---LIYNKALVDQPPETTDELLAIMKD 139
|
|
| PotD |
COG0687 |
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
5-181 |
3.53e-03 |
|
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 39.51 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 5 KKLAFTGVSALLLGTLAACGGSGskdqaeASNSDTLQMYQIGDkpdNFDQlmEVAnKRIEKEIGVKVNINYIG-WGDYEK 83
Cdd:COG0687 2 SRRSLLGLAAAALAAALAGGAPA------AAAEGTLNVYNWGG---YIDP--DVL-EPFEKETGIKVVYDTYDsNEEMLA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 84 KMNviiSSGENYDIAFANNYVSN--AQKGAFA--DLTELapkyaeKAYNDLDEAYIKGNLVNGKLYAFPVNGNVFaqqVL 159
Cdd:COG0687 70 KLR---AGGSGYDVVVPSDYFVArlIKAGLLQplDKSKL------PNLANLDPRFKDPPFDPGNVYGVPYTWGTT---GI 137
|
170 180
....*....|....*....|..
gi 488214766 160 TFNKALLDKydlsidGIQSYAD 181
Cdd:COG0687 138 AYNTDKVKE------PPTSWAD 153
|
|
| NlpA |
COG1464 |
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion ... |
5-132 |
7.89e-03 |
|
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion transport and metabolism];
Pssm-ID: 441073 [Multi-domain] Cd Length: 270 Bit Score: 38.17 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 5 KKLAFTGVSALLLGTLAACGGSGSKDQAEASNsdTLqmyQIGDKPDNFDQLMEVANKRIEKEiGVKVNInyIGWGDYeKK 84
Cdd:COG1464 2 KKLLALLLALALALALAACGSSSAAAAAADKK--TI---KVGATPGPHAEILEVVKPELAKK-GIDLEI--VEFTDY-VQ 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488214766 85 MNVIISSGE---NYD--IAFANNYvsNAQKGafADLTELAPKYAE------KAYNDLDE 132
Cdd:COG1464 73 PNEALADGEidaNYFqhIPYLDNF--NKENG--YDLVPVGKTHIEpmglysKKYKSLDE 127
|
|
| malE |
PRK09474 |
maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
1-166 |
8.53e-03 |
|
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 38.45 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 1 MKLWKKLAFTGVSALLLGTLAACggsgskdqaeASNSDTLQMYQIGDKpdNFDQLMEVAnKRIEKEIGVKVNINYIGwgD 80
Cdd:PRK09474 4 KKGLRTLALSALATLMFSASALA----------KIEEGKLVIWINGDK--GYNGLAEVG-KKFEKDTGIKVTVEHPD--K 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488214766 81 YEKKMNVIISSGENYDIAF--ANNYVSNAQKGAFADLT---ELAPKYAEKAYNDLDeayikgnlVNGKLYAFPVNGNVFA 155
Cdd:PRK09474 69 LEEKFPQVAATGDGPDIIFwaHDRFGGYAQSGLLAEVTpskAFKDKLVPFTWDAVR--------YNGKLIGYPIAVEALS 140
|
170
....*....|.
gi 488214766 156 qqvLTFNKALL 166
Cdd:PRK09474 141 ---LIYNKDLV 148
|
|
| |
